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J Biol Chem, Vol. 274, Issue 16, 11209-11219, April 16, 1999
From the Department of Biomolecular Chemistry, University of
Wisconsin, Madison, Wisconsin 53706-1532
To evaluate the mechanisms by which
epidermal growth factor (EGF) regulates actin-based cellular
processes such as cell migration, we first examined the
effects of EGF on cell adhesion, which is essential for cell
migration. In mouse B82L fibroblasts transfected with the full-length
EGF receptor, EGF promotes cell rounding and attenuates cell spreading
on fibronectin, laminin, and vitronectin, and thus appears to reduce
the strength of cell adhesion. Moreover, EGF synergizes with multiple
extracellular matrix (ECM) components in the promotion of
integrin-mediated cell migration of several different cell types,
including fibroblasts and various carcinoma and osteosarcoma cell
lines. Interestingly, co-presentation (co-positioning) of EGF with
laminin or fibronectin is essential for EGF-stimulated migration. When
EGF is mixed with the cells instead of the ECM components, it has
little effect on cell migration. These results suggest that
co-presentation of EGF with ECM components can enhance the polarization
events required for directional cell movement. To identify the EGF
receptor elements critical for the EGF stimulation of cell migration,
B82L fibroblasts were transfected with either mutated or wild-type EGF
receptors. Surprisingly, we found that B82L-Parental cells that lack
the EGF receptor are not able to migrate to fibronectin, even though
they can adhere to fibronectin. However, the introduction of wild-type
EGF receptors into these fibroblasts enables them to migrate toward
fibronectin even in the absence of EGF. The requirement of the EGF
receptor for cell migration does not appear to result from the
secretion of EGF or TGF-
Integrin-mediated Migration of Murine B82L Fibroblasts Is
Dependent on the Expression of an Intact Epidermal Growth Factor
Receptor
by the cells transfected with the EGF
receptor. Furthermore, cells expressing EGF receptors that are
kinase-inactive, or C-terminally truncated, exhibit little migration
toward fibronectin, indicating that an intact EGF receptor kinase is
required for fibronectin-induced cell migration. In addition,
neutralizing anti-EGF receptor antibodies attenuate cell migration in
the presence of EGF, and inhibit migration to fibronectin or laminin
alone. These results further suggest that the EGF receptor is
downstream of integrin activation in the signal transduction pathways
leading to fibroblast migration.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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